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Journal of Chemistry
Volume 2017, Article ID 8756519, 6 pages
https://doi.org/10.1155/2017/8756519
Research Article

The Adhesion Mechanism of Marine Mussel Foot Protein: Adsorption of L-Dopa on - and -Cristobalite Silica Using Density Functional Theory

Department of Physics, University of Peshawar, Peshawar, Pakistan

Correspondence should be addressed to Shabeer Ahmad Mian; kp.ude.hsepu@damhareebahs

Received 28 August 2016; Revised 20 November 2016; Accepted 21 December 2016; Published 15 January 2017

Academic Editor: Anton Kokalj

Copyright © 2017 Shabeer Ahmad Mian and Younas Khan. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Abstract

Marine mussels strongly adhere to various surfaces and endure their attachment under a variety of conditions. In order to understand the basic mechanism involved, we study the adsorption of L-dopa molecule on hydrophilic geminal and terminal isolated silanols of silica (001) surface. High content of modified amino acid L-dopa is found in the glue-like material secreted by the mussels through which it sticks to various surfaces under water. To understand the adsorption behavior, we have made use of periodic Density Functional Theory (DFT) study. The L-dopa molecule adheres to silica surfaces terminated with geminal and terminal silanols via its catechol part. In both cases, the adhesion is achieved through the formation of 4 H-bonds. A binding energy of 29.48 and 31.67 kcal/mol has been estimated, after the inclusion of dispersion energy, for geminal and terminal silanols of silica, respectively. These results suggest a relatively stronger adhesion of dopa molecule for surface with terminal isolated silanols.